Ph-dependent interactions and the stability and folding kinetics of the N-terminal domain of L9. electrostatic interactions are only weakly formed in the transition state for folding 1 1Edited by C. R. Matthews

Analysis of the pH-dependent stability and millisecond folding kinetics of horse cytochrome c

“…The terms Dn (pH) and Dn z (pH) represent the difference in the number of protons bound to the folded and unfolded states, and transition and unfolded states, respectively. In accordance with few earlier studies [17,47,51,53], the development of electrostatic interactions in the transition state for folding can be quantitatively measured by comparison of the ratio: were attributed to lesser development of electrostatic interactions in the transition states for folding of these two proteins [52,59].…”

“…In general, if the electrostatic interactions are poorly formed in the transition state then the variation in pH will alter the stability of the folded state more than the stability of the transition state [52]. In this scenario, the unfolding rate is likely to change significantly with pH, while only small change in the folding rate is expected.…”

“…Fig. 5 C presents the GdnHCl-dependence of the logarithm of observed refolding and unfolding rates of Ferrocyt c measured at pH 7.0 and pH 12.7 at 25 C. Our previous extensive equilibrium and millisecond kinetic folding studies of Ferrocyt c revealed that the folding kinetics of Ferrocyt c is two-state [70], so in the current manuscript the dependency of Log k obs on GdnHCl concentration was analyzed according to two-state model, N#U [52],…”

“…Fersht and coworkers have analyzed the pHdependence of folding and unfolding kinetics of CI-2 and barnase [59]. The pioneering works by Raleigh and coworkers have shown that the comparison of pH-dependent protein stability profiles and folding rates can provide information about the development of electrostatic interactions in transition state of folding [52,56,58].…”

BIOTECHNOLOGY: Aggregation of Recombinant Human Botulinum Protein Antigen Serotype C in Varying Solution Conditions: Implications of Conformational Stability for Aggregation Kinetics

“…Differences in G H 2 O values obtained for different solution conditions are related not only to the conformational stability of the native state but are also affected by differences in the degree of unfolding of the denatured state, which can vary as a function of solution pH. [31][32][33][34][35] If the properties of the unfolded state are changing appreciably across the range of solution conditions, the use of G H 2 O alone as a predictor of the size of the population of reactive, partially unfolded species might not be valid. Figure 7.…”